ID A0A090HY48_9FIRM Unreviewed; 177 AA.
AC A0A090HY48;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Signal peptidase I {ECO:0000256|RuleBase:RU362042};
DE EC=3.4.21.89 {ECO:0000256|RuleBase:RU362042};
GN Name=spsB {ECO:0000313|EMBL:CDZ75132.1};
GN ORFNames=ING2D1G_0992 {ECO:0000313|EMBL:CDZ75132.1};
OS Peptoniphilus sp. ING2-D1G.
OC Bacteria; Bacillota; Tissierellia; Tissierellales; Peptoniphilaceae;
OC Peptoniphilus.
OX NCBI_TaxID=1912856 {ECO:0000313|EMBL:CDZ75132.1, ECO:0000313|Proteomes:UP000032409};
RN [1] {ECO:0000313|EMBL:CDZ75132.1, ECO:0000313|Proteomes:UP000032409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Peptoniphilus sp. ING2-D1G {ECO:0000313|Proteomes:UP000032409};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences
CC from secreted and periplasmic proteins.; EC=3.4.21.89;
CC Evidence={ECO:0000256|RuleBase:RU362042};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC Membrane {ECO:0000256|ARBA:ARBA00004606,
CC ECO:0000256|RuleBase:RU362042}; Single-pass type II membrane protein
CC {ECO:0000256|ARBA:ARBA00004606, ECO:0000256|RuleBase:RU362042}.
CC -!- SIMILARITY: Belongs to the peptidase S26 family.
CC {ECO:0000256|ARBA:ARBA00009370, ECO:0000256|RuleBase:RU362042}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LM997412; CDZ75132.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A090HY48; -.
DR STRING; 1912856.ING2D1G_0992; -.
DR KEGG; ped:ING2D1G_0992; -.
DR PATRIC; fig|875453.3.peg.934; -.
DR HOGENOM; CLU_028723_5_1_9; -.
DR OrthoDB; 9802919at2; -.
DR Proteomes; UP000032409; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro.
DR CDD; cd06530; S26_SPase_I; 1.
DR Gene3D; 2.10.109.10; Umud Fragment, subunit A; 1.
DR InterPro; IPR036286; LexA/Signal_pep-like_sf.
DR InterPro; IPR000223; Pept_S26A_signal_pept_1.
DR InterPro; IPR019533; Peptidase_S26.
DR NCBIfam; TIGR02227; sigpep_I_bact; 1.
DR PANTHER; PTHR43390:SF1; CHLOROPLAST PROCESSING PEPTIDASE; 1.
DR PANTHER; PTHR43390; SIGNAL PEPTIDASE I; 1.
DR Pfam; PF10502; Peptidase_S26; 1.
DR PRINTS; PR00727; LEADERPTASE.
DR SUPFAM; SSF51306; LexA/Signal peptidase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|RuleBase:RU362042, ECO:0000313|EMBL:CDZ75132.1};
KW Protease {ECO:0000256|RuleBase:RU362042};
KW Reference proteome {ECO:0000313|Proteomes:UP000032409}.
FT DOMAIN 9..167
FT /note="Peptidase S26"
FT /evidence="ECO:0000259|Pfam:PF10502"
FT ACT_SITE 39
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
FT ACT_SITE 82
FT /evidence="ECO:0000256|PIRSR:PIRSR600223-1"
SQ SEQUENCE 177 AA; 20425 MW; 119AF238375497FE CRC64;
MKEKKESLMN YIFMFAIAII LALLIRHFVF TSNIVSGVSM EPSFQNNDRL IALVFPLYLK
DPEYSDVVII ESPIEENKEY IKRIIAKPRD NVLIENGSVY VNGNKLNEPY IEQGVETQIY
NDFFWTLDEN QYFVLGDNRN PGKSSDSRVF GPIEREAIKG IVKFRFWPLS KFGVIGG
//